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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2010-3-12
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pubmed:abstractText |
The centrosome is the primary microtubule organizing centre of the cell. gamma-tubulin is a core component of the centrosome and is required for microtubule nucleation and centrosome function. The recruitment of gamma-tubulin to centrosomes is mediated by its interaction with NEDD1, a WD40-repeat containing protein. Here we demonstrate that NEDD1 is likely to be oligomeric in vivo and binds directly to gamma-tubulin through a small region of just 62 residues at the carboxyl-terminus of the protein. This carboxyl-terminal domain that binds gamma-tubulin has a helical structure and is a stable tetramer in solution. Mutation of residues in NEDD1 that disrupt binding to gamma-tubulin result in a mis-localization of gamma-tubulin away from the centrosome. Hence, this study defines the binding site on NEDD1 that is required for its interaction with gamma-tubulin, and shows that this interaction is required for the correct localization of gamma-tubulin.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-10212229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-10322210,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-11533726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-11694571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-15252135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-16212501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-16378099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-16461362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-17005434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-17959831,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-17980596,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-18207742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-18239929,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-18252801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-18776082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-19029337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-19243593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-19509060,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-19536135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-19543530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-19596795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-4366945,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20224777-8157664
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e9618
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pubmed:meshHeading |
pubmed-meshheading:20224777-Animals,
pubmed-meshheading:20224777-Binding Sites,
pubmed-meshheading:20224777-Cell Line,
pubmed-meshheading:20224777-Centrosome,
pubmed-meshheading:20224777-Circular Dichroism,
pubmed-meshheading:20224777-Humans,
pubmed-meshheading:20224777-Mice,
pubmed-meshheading:20224777-Microtubule-Associated Proteins,
pubmed-meshheading:20224777-Mutation,
pubmed-meshheading:20224777-NIH 3T3 Cells,
pubmed-meshheading:20224777-Protein Binding,
pubmed-meshheading:20224777-Protein Structure, Tertiary,
pubmed-meshheading:20224777-Scattering, Radiation,
pubmed-meshheading:20224777-Tubulin
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pubmed:year |
2010
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pubmed:articleTitle |
A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome.
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pubmed:affiliation |
Centre for Cancer Biology, SA Pathology, Adelaide, South Australia, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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